ID   HEMZ_RHOS4              Reviewed;         450 AA.
AC   P51008; Q3J009;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 55.
DE   RecName: Full=Coproporphyrinogen III oxidase, anaerobic 2;
DE            Short=Coproporphyrinogenase;
DE            Short=Coprogen oxidase;
DE            EC=1.3.99.22;
GN   Name=hemZ; OrderedLocusNames=RHOS4_23070; ORFNames=RSP_0699;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96062223; PubMed=7592416;
RA   Zeilstra-Ryalls J.H., Kaplan S.;
RT   "Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1:
RT   the role of the fnrL gene.";
RL   J. Bacteriol. 177:6422-6431(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Anaerobic transformation of coproporphyrinogen-III into
CC       protoporphyrinogen-IX. Dedicated to bacteriochlorophyll
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L-
CC       methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2
CC       5'-deoxyadenosine.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       protoporphyrinogen-IX from coproporphyrinogen III (AdoMet route):
CC       step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen III
CC       oxidase family.
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DR   EMBL; Z49746; CAA89819.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA79875.1; -; Genomic_DNA.
DR   RefSeq; YP_353776.1; -.
DR   GeneID; 3718177; -.
DR   GenomeReviews; CP000143_GR; RHOS4_23070.
DR   KEGG; rsp:RSP_0699; -.
DR   NMPDR; fig|272943.3.peg.3048; -.
DR   HOGENOM; P51008; -.
DR   BioCyc; RSPH272943:RSP_0699-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:EC.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR004558; HemN.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR007197; Radical_SAM.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00538; hemN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW   Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW   Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine.
FT   CHAIN         1    450       Coproporphyrinogen III oxidase, anaerobic
FT                                2.
FT                                /FTId=PRO_0000109950.
FT   REGION      112    113       S-adenosyl-L-methionine 2 binding (By
FT                                similarity).
FT   METAL        60     60       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        64     64       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        67     67       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   BINDING      54     54       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      66     66       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     111    111       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     144    144       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING     171    171       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     183    183       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     208    208       S-adenosyl-L-methionine 2 (By
FT                                similarity).
SQ   SEQUENCE   450 AA;  49103 MW;  CD391AB6F80BBA3E CRC64;
     MAAVSHLAKL GLFDARVPRY TSYPTAPNFG VGVTENLHAD WISSIPAGGS ISLYLHVPFC
     RRLCWFCACR TQGTSSDAPV RAYAAALKSE LALLRARLAP GVRLARMHWG GGTPTLLPPT
     LIHELALAIR DAVPSDAETD FSVEIDPTEI DAARLDALFE AGMTRVSIGV QDFDPLIQQS
     IGREQSFELT QRLTEDLRHR GLMGLDADIL YGLPHQTAPG VADSVQKLLS LSPDRVAVLG
     YAHVPAVSRR QLMIPTASIP GPEERLDLFE TARTLILWDG YQQVGLDHFA RAGDPLAHAH
     ACGRLCRSFQ GYTDDRAEVL IGLGASAISR FPQGFTQNAP STSDHLRAIR SGRFSTARGH
     VLSDEDRLRG RMIEQLLCEF RISRAQILAR FAVAPERLET LFRTCAAAFP GVVEITGHGL
     EILEEGRPLA RIVARSFDRY DASGKPQGAI
//